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P56716

- RP1_MOUSE

UniProt

P56716 - RP1_MOUSE

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Protein

Oxygen-regulated protein 1

Gene

Rp1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Microtubule-associated protein regulating the stability and length of the microtubule-based axoneme of photoreceptors. Required for the differentiation of photoreceptor cells, it plays a role in the organization of the outer segment of rod and cone photoreceptors ensuring the correct orientation and higher-order stacking of outer segment disks along the photoreceptor axoneme.2 Publications

GO - Molecular functioni

  1. microtubule binding Source: UniProtKB

GO - Biological processi

  1. axoneme assembly Source: UniProtKB
  2. cellular response to light stimulus Source: MGI
  3. intracellular signal transduction Source: InterPro
  4. microtubule polymerization Source: BHF-UCL
  5. negative regulation of microtubule depolymerization Source: BHF-UCL
  6. photoreceptor cell development Source: UniProtKB
  7. photoreceptor cell maintenance Source: UniProtKB
  8. photoreceptor cell outer segment organization Source: UniProtKB
  9. retina development in camera-type eye Source: MGI
  10. retinal cone cell development Source: UniProtKB
  11. retinal rod cell development Source: UniProtKB
  12. retina morphogenesis in camera-type eye Source: MGI
  13. visual perception Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cilium biogenesis/degradation, Sensory transduction, Vision

Names & Taxonomyi

Protein namesi
Recommended name:
Oxygen-regulated protein 1
Alternative name(s):
Retinitis pigmentosa RP1 protein homolog
Gene namesi
Name:Rp1
Synonyms:Orp1, Rp1h
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:1341105. Rp1.

Subcellular locationi

Cytoplasmcytoskeletoncilium axoneme. Cell projectionciliumphotoreceptor outer segment
Note: Specifically localized in the connecting cilia of rod and cone photoreceptors.

GO - Cellular componenti

  1. axoneme Source: UniProtKB
  2. cilium Source: MGI
  3. microtubule associated complex Source: UniProtKB
  4. photoreceptor connecting cilium Source: UniProtKB
  5. photoreceptor inner segment Source: UniProtKB
  6. photoreceptor outer segment Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Disruption phenotypei

As early as postnatal day 7, mice have already undergone significant molecular retinal changes. The molecular responses change dramatically during development and were distinct from responses to the disruption of the photoreceptor transcription factors Crx, Pde6b and Nrl. The JNK signaling cascades are specifically compromised in Rp1 defective retinas. Double heterozygotes of Rp1 and Rp1l1 exhibit abnormal outer segment morphology and reduced single rod photosensitivity and dark currents.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20952095Oxygen-regulated protein 1PRO_0000097411Add
BLAST

Proteomic databases

PaxDbiP56716.
PRIDEiP56716.

PTM databases

PhosphoSiteiP56716.

Expressioni

Tissue specificityi

Expressed in the cell bodies and inner segments of photoreceptors. Not found in liver, spleen, kidney, brain, thymus, muscle, heart, lung and testis.

Inductioni

Gene expression is stimulated by retinal hypoxia and suppressed by relative retinal hyperoxia.

Gene expression databases

BgeeiP56716.
CleanExiMM_RP1H.
ExpressionAtlasiP56716. differential.
GenevestigatoriP56716.

Interactioni

Subunit structurei

Interacts (via the doublecortin domains) with microtubules. Interacts with RP1L1. Interacts with MAK.3 Publications

Protein-protein interaction databases

DIPiDIP-59493N.
IntActiP56716. 1 interaction.
MINTiMINT-4132931.
STRINGi10090.ENSMUSP00000111202.

Structurei

3D structure databases

ProteinModelPortaliP56716.
SMRiP56716. Positions 34-108.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 11783Doublecortin 1PROSITE-ProRule annotationAdd
BLAST
Domaini157 – 23680Doublecortin 2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi655 – 6606Poly-Lys

Domaini

The doublecortin domains, which mediate interaction with microtubules, are required for regulation of microtubule polymerization and function in photoreceptor differentiation.By similarity

Sequence similaritiesi

Contains 2 doublecortin domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG313727.
GeneTreeiENSGT00530000063898.
HOGENOMiHOG000136857.
HOVERGENiHBG018173.
InParanoidiP56716.
OMAiEYHMFTH.
OrthoDBiEOG7N37DH.
PhylomeDBiP56716.
TreeFamiTF318770.

Family and domain databases

Gene3Di3.10.20.230. 2 hits.
InterProiIPR003533. Doublecortin_dom.
[Graphical view]
PfamiPF03607. DCX. 2 hits.
[Graphical view]
SMARTiSM00537. DCX. 2 hits.
[Graphical view]
PROSITEiPS50309. DC. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P56716-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSDTPSTSFS MIHLTSEGQV PSPRHSNITH PVVAKRISFY KSGDPQFGGV
60 70 80 90 100
RVVVNPRSFK TFDALLDSLS RKVPLPFGVR NISTPRGRHS ITRLEELEDG
110 120 130 140 150
KSYVCSHNKK VLPVDLDKAR RRPRPWLSSR SISTHVQLCP ATANMSTMAP
160 170 180 190 200
GMLRAPRRLV VFRNGDPKNK HVVLLSRRIT QSFEAFLQYL TQVMQCPVAK
210 220 230 240 250
LYATDGRKVP SLQAVILSSG AVVAAGREPF KPGNYDIQKY LLPAKLPGIS
260 270 280 290 300
HRVHQKGKAK IEKRKMSTHM PSDLRPQTDS LISEKTYDCF SDFSVAPENY
310 320 330 340 350
LALETHESQS LSTYPSEDDV EKSIVFNQDG TMTVVMKVRF KIKEEETVKW
360 370 380 390 400
TTTVNRAGLS NNDEKNKKSS YPGKTDYGPS SLKLEACSLP EDIVDTTQQG
410 420 430 440 450
SLTEEENTQM TEQQALSCSS ASWENASMET DIQESQKQVK HFYRPPTPGP
460 470 480 490 500
RRMRQKKSVI GTVTVVSETE VQEKQFSYSE ERKGGEKSEY HMFTHSCSKM
510 520 530 540 550
SSVSNKLVQI GSDNEMESAL ERTRESGSLK SQAINAGAIE ITSQKVLKMC
560 570 580 590 600
HNNALPSTAP ENSVVEEGTD NSAVSGTATI KHFRTCGNAN DSFSSITADS
610 620 630 640 650
TPTSVNNYSN DRNISELPSV GSPVLTMRLV NEFAHCGLTE KPENRKKVLS
660 670 680 690 700
SSASKKKKKK SQQRMITSND KKKVIETKGP PNIAGKIPRA GTTAQERLLQ
710 720 730 740 750
ESDCPDKGGR VCEQGLNISP MAIESNNFFP KSNPTFSKNF YKNKLNTFQN
760 770 780 790 800
PKTQKLLAKR KSRPRKIVST ERLRKQEIGQ EDKILLHSDS KLCESHLEKQ
810 820 830 840 850
SLFHVFNILE EDQKVLHRPP FQVEKVARNL KGMAKKSLVP KVNDLHIMLR
860 870 880 890 900
NQKKQMGVKL KSGAEVSEQH VTTRADPLAS LKKPDFPEGI PHHSGKSYVK
910 920 930 940 950
RWLQNINSYP DFEHRKSGPL CQNRSDVVNY NRNGFLGNNL HTTSSKGNGF
960 970 980 990 1000
LMESNKSKTK NDNWSGNTNQ ETGKSLVAKD NGEELNKHHC ESQNGSLYDS
1010 1020 1030 1040 1050
YLVSLHDNCT LSQTTINEPS TKSHLSIEKS RPEVKLVYQE MNFATKRQSI
1060 1070 1080 1090 1100
EVAIQVDTMG ENVLKDYLPA LLLRHLEAFV PNNQKHQNGI SQIPGSLAEV
1110 1120 1130 1140 1150
VFPSVIDNSS TNLLLAWLLV LNLKRTMNSF CQSDAHKMTN RPSETAALLE
1160 1170 1180 1190 1200
VLKHVAITEE ADDLKAAVAN LMESTKTCSG SSGREQDMLP VNCTASSLHS
1210 1220 1230 1240 1250
VDECNENGSA QKTLLDEGYS VMGDCTSEMV SKSCNSSCEM HMVSKTNPPK
1260 1270 1280 1290 1300
QVDDQSDGLL TSNSCTVSQR STGACFLTDG VYSHEACAQK EGVYEGACLS
1310 1320 1330 1340 1350
DETHIPIRDC HTIHSVHSKE NKCTDDLEST EELKTVDKVP KGLSILADSM
1360 1370 1380 1390 1400
YKNDSNVSTF QNVNKLSSQR TLLSKTYLDS DKDYSPLEEF QNCPRKKIVN
1410 1420 1430 1440 1450
KKKSISSDKE ESRTSEEPRS ITNSMTSSER NAISELESFE ELESQDTSIF
1460 1470 1480 1490 1500
NMNVRAEKKS TKETMQKQSE ARMSSELINV SGRKIIEQER RNTAILETTA
1510 1520 1530 1540 1550
RGQVTPPSLA FCYDSNKNTE KEISEGETKM RVKKMVDSME NESYSESSLN
1560 1570 1580 1590 1600
FKKHHRSPGT LDWSDYGSDS ESGYPCKASS NSHNDDSGQE KEPTRGIVKR
1610 1620 1630 1640 1650
AIEKLYGKAE IIKPPFFHGS IHKSQVCPYN SVEVQCAKKT NFYESECQSL
1660 1670 1680 1690 1700
VSSEQVSRSS LIFQEFPQVD ANGMGDSFGD SSIENVTKSS AHDRVFTEKE
1710 1720 1730 1740 1750
NGKLIDNGKW LLRENHLWRV SSDNPGMYGN ADTTSVDTLI DKNSIEVPYS
1760 1770 1780 1790 1800
HFGELAPGPT MAELSSSEIE EMTQPLEVKC NYFNFPHGSD SEPFGEDFPD
1810 1820 1830 1840 1850
AQNKTCPKEK IPNHHTEEKG NYPSERLCTS VTQAFVSAGN KVHPVCSDAI
1860 1870 1880 1890 1900
KTQPLPGSNI THGALQEGDS LDKLYALCGQ HCPILTVIIQ PVNEESRGFA
1910 1920 1930 1940 1950
YRKDSDIENS LDFQLWMKIY PFMPQSKKHV FRSDGRNVSV GEEFAGNVIG
1960 1970 1980 1990 2000
DLCDQLYFKS MIDLVDQRAN SLGKEINLKK FQLYLKKSFS DPLSTSLLVV
2010 2020 2030 2040 2050
ENRNSVSLSP SSWTDNFKSI DENNNFLNRL PNSSKNPNQV VRENTNFQFH
2060 2070 2080 2090
LELFGQVYLL DICQVEKPLN IKTRSKLEMY YILEGEVLFI WEEEK
Length:2,095
Mass (Da):234,388
Last modified:June 6, 2002 - v2
Checksum:iCA5301316633BD62
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF155141 mRNA. Translation: AAD42089.2.
AF291754 Genomic DNA. Translation: AAM17919.1.
BC120927 mRNA. Translation: AAI20928.1.
BC120928 mRNA. Translation: AAI20929.1.
CCDSiCCDS14804.1.
RefSeqiNP_035413.1. NM_011283.2.
UniGeneiMm.294263.

Genome annotation databases

EnsembliENSMUST00000027032; ENSMUSP00000027032; ENSMUSG00000025900.
GeneIDi19888.
KEGGimmu:19888.
UCSCiuc007aex.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF155141 mRNA. Translation: AAD42089.2 .
AF291754 Genomic DNA. Translation: AAM17919.1 .
BC120927 mRNA. Translation: AAI20928.1 .
BC120928 mRNA. Translation: AAI20929.1 .
CCDSi CCDS14804.1.
RefSeqi NP_035413.1. NM_011283.2.
UniGenei Mm.294263.

3D structure databases

ProteinModelPortali P56716.
SMRi P56716. Positions 34-108.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-59493N.
IntActi P56716. 1 interaction.
MINTi MINT-4132931.
STRINGi 10090.ENSMUSP00000111202.

PTM databases

PhosphoSitei P56716.

Proteomic databases

PaxDbi P56716.
PRIDEi P56716.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000027032 ; ENSMUSP00000027032 ; ENSMUSG00000025900 .
GeneIDi 19888.
KEGGi mmu:19888.
UCSCi uc007aex.2. mouse.

Organism-specific databases

CTDi 6101.
MGIi MGI:1341105. Rp1.

Phylogenomic databases

eggNOGi NOG313727.
GeneTreei ENSGT00530000063898.
HOGENOMi HOG000136857.
HOVERGENi HBG018173.
InParanoidi P56716.
OMAi EYHMFTH.
OrthoDBi EOG7N37DH.
PhylomeDBi P56716.
TreeFami TF318770.

Miscellaneous databases

NextBioi 297400.
PROi P56716.
SOURCEi Search...

Gene expression databases

Bgeei P56716.
CleanExi MM_RP1H.
ExpressionAtlasi P56716. differential.
Genevestigatori P56716.

Family and domain databases

Gene3Di 3.10.20.230. 2 hits.
InterProi IPR003533. Doublecortin_dom.
[Graphical view ]
Pfami PF03607. DCX. 2 hits.
[Graphical view ]
SMARTi SM00537. DCX. 2 hits.
[Graphical view ]
PROSITEi PS50309. DC. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mutations in a gene encoding a new oxygen-regulated photoreceptor protein cause dominant retinitis pigmentosa."
    Pierce E.A., Quinn T., Meehan T., McGee T.L., Berson E.L., Dryja T.P.
    Nat. Genet. 22:248-254(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SEQUENCE REVISION TO 67-76.
    Tissue: Retina.
  2. "Progressive photoreceptor degeneration, outer segment dysplasia, and rhodopsin mislocalization in mice with targeted disruption of the retinitis pigmentosa-1 (Rp1) gene."
    Gao J., Cheon K., Nusinowitz S., Liu Q., Bei D., Atkins K., Azimi A., Daiger S.P., Farber D.B., Heckenlively J.R., Pierce E.A., Sullivan L.S., Zuo J.
    Proc. Natl. Acad. Sci. U.S.A. 99:5698-5703(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/Sv.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 357-367, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  5. "Identification and subcellular localization of the RP1 protein in human and mouse photoreceptors."
    Liu Q., Zhou J., Daiger S.P., Farber D.B., Heckenlively J.R., Smith J.E., Sullivan L.S., Zuo J., Milam A.H., Pierce E.A.
    Invest. Ophthalmol. Vis. Sci. 43:22-32(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  6. Cited for: FUNCTION, SUBCELLULAR LOCATION.
  7. "The retinitis pigmentosa 1 protein is a photoreceptor microtubule-associated protein."
    Liu Q., Zuo J., Pierce E.A.
    J. Neurosci. 24:6427-6436(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MICROTUBULES, SUBCELLULAR LOCATION.
  8. "Distinct gene expression profiles and reduced JNK signaling in retinitis pigmentosa caused by RP1 mutations."
    Liu J., Huang Q., Higdon J., Liu W., Xie T., Yamashita T., Cheon K., Cheng C., Zuo J.
    Hum. Mol. Genet. 14:2945-2958(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  9. "Essential and synergistic roles of RP1 and RP1L1 in rod photoreceptor axoneme and retinitis pigmentosa."
    Yamashita T., Liu J., Gao J., LeNoue S., Wang C., Kaminoh J., Bowne S.J., Sullivan L.S., Daiger S.P., Zhang K., Fitzgerald M.E., Kefalov V.J., Zuo J.
    J. Neurosci. 29:9748-9760(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RP1L1, DISRUPTION PHENOTYPE.
  10. "Negative regulation of ciliary length by ciliary male germ cell-associated kinase (Mak) is required for retinal photoreceptor survival."
    Omori Y., Chaya T., Katoh K., Kajimura N., Sato S., Muraoka K., Ueno S., Koyasu T., Kondo M., Furukawa T.
    Proc. Natl. Acad. Sci. U.S.A. 107:22671-22676(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAK.

Entry informationi

Entry nameiRP1_MOUSE
AccessioniPrimary (citable) accession number: P56716
Secondary accession number(s): Q548Q8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 6, 2002
Last modified: October 29, 2014
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3